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Purification and characterization of a human brain galectin-1 ligand.
- Source :
-
Journal of neurochemistry [J Neurochem] 1997 Apr; Vol. 68 (4), pp. 1640-7. - Publication Year :
- 1997
-
Abstract
- Our previous studies have characterized an endogenous lectin from human brain identified as galectin-1. A soluble ligand of galectin-1 was purified from human brain by affinity chromatography and preparative electrophoresis. The purified ligand (termed HBGp82, for human brain galectin-1-binding polypeptide of 82,000 daltons) has an apparent molecular mass of 82 kDa and is glycosylated by N-linked biantennary complex structures. HBGp82 was partially characterized by microsequencing of peptide fragments. Similar peptides were found in a heat shock of protein of 90,000 daltons, hsp90. However, comparison of apparent molecular weights and matrix-assisted laser desorption mass spectrometry clearly showed that HBGp82 differs to some degree from hsp90.
- Subjects :
- Amino Acid Sequence
Chromatography, High Pressure Liquid
Galectin 1
Glycosylation
Hemagglutinins isolation & purification
Hemagglutinins metabolism
Humans
Lectins analysis
Lectins isolation & purification
Lectins metabolism
Ligands
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Neuropeptides analysis
Neuropeptides isolation & purification
Neuropeptides metabolism
Brain Chemistry
Hemagglutinins analysis
Subjects
Details
- Language :
- English
- ISSN :
- 0022-3042
- Volume :
- 68
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Journal of neurochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 9084436
- Full Text :
- https://doi.org/10.1046/j.1471-4159.1997.68041640.x